U.S. patent application number 14/810977 was filed with the patent office on 2017-02-02 for sheet packs for treating facial or body surfaces.
The applicant listed for this patent is ELC Management LLC. Invention is credited to Anne Carullo, Donald Collins, Osvaldo Fontanet, Allan Hafkin, Joyce Kassouf, Dawn Layman, Jennifer Palmer Quintano, Nadine Pernodet.
Application Number | 20170027878 14/810977 |
Document ID | / |
Family ID | 57885336 |
Filed Date | 2017-02-02 |
United States Patent
Application |
20170027878 |
Kind Code |
A1 |
Carullo; Anne ; et
al. |
February 2, 2017 |
Sheet Packs For Treating Facial Or Body Surfaces
Abstract
A sheet pack comprising an absorbent layer impregnated with a
treatment composition containing at least one ingredient that when
topically applied to skin stimulates a gene that is variably
expressed over a 24 hour period in native untreated skin cells; the
sheet pack contained in a package with user instructions to
topically apply the sheet pack to the skin at a time when the gene
that is stimulated by the ingredient is being maximally expressed
in native untreated skin cells; and methods for treating skin and
methods for making a sheet pack.
Inventors: |
Carullo; Anne; (New York,
NY) ; Palmer Quintano; Jennifer; (New York, NY)
; Kassouf; Joyce; (New York, NY) ; Pernodet;
Nadine; (Huntington Station, NY) ; Collins;
Donald; (Plainview, NY) ; Layman; Dawn;
(Ridge, NY) ; Hafkin; Allan; (Plainview, NY)
; Fontanet; Osvaldo; (Emerson, NJ) |
|
Applicant: |
Name |
City |
State |
Country |
Type |
ELC Management LLC |
Melville |
NY |
US |
|
|
Family ID: |
57885336 |
Appl. No.: |
14/810977 |
Filed: |
July 28, 2015 |
Current U.S.
Class: |
1/1 |
Current CPC
Class: |
A45D 44/002 20130101;
A61L 2300/25 20130101; A61K 8/64 20130101; A61K 36/28 20130101;
A61K 9/7007 20130101; A61K 9/70 20130101; A61K 36/18 20130101; A61K
9/7023 20130101; A45D 44/22 20130101; A61K 8/0212 20130101; A61P
43/00 20180101; A61Q 19/08 20130101; A61K 8/36 20130101; A61L 15/44
20130101 |
International
Class: |
A61K 9/70 20060101
A61K009/70; A61K 36/28 20060101 A61K036/28 |
Claims
1. A sheet pack comprising an absorbent layer impregnated with a
treatment composition containing at least one ingredient that when
topically applied to skin stimulates a gene that is variably
expressed over a 24 hour period in native untreated skin cells; the
sheet pack contained in a package with user instructions to
topically apply the sheet pack to the skin at a select time period
within the 24 hour time period when the same gene that is
stimulated by the ingredient is being maximally expressed in native
untreated skin cells.
2. The sheet pack of claim 1 wherein the gene that is variably
expressed in native untreated skin cells is one or more of Period
gene 1, 2, or 3 (PER1, 2, 3); Circadian Locomotor Output Cycles
Kaput (CLOCK) gene; Brain and Muscle Arylhydrocarbon Receptor
Nuclear Translocator (BMAL) gene; or cryptochrome circadian gene
(CRY).
3. The sheet pack of claim 2 wherein the sheet pack is in the form
of a laminate with an impermeable layer bonded to the absorbent
layer.
4. The sheet pack of claim 3 wherein the absorbent layer is a
non-woven fabric and the impermeable layer is a metallic foil.
5. The sheet pack of claim 4 wherein the absorbent layer is a
non-woven fabric having one or more of the following
specifications: (a) absorbs water from 0.03 to 2.5 ml/gram after 5
seconds per 1 gram measured by the Larose method, (b) a thickness a
thickness ranging from 0.1 to 1.0 mm, (c) a bending resistance of
1.0 to 2.0 mmm.sup.2/gram, (d) a drape co-efficient ranging from 1
to 70%, (e) a KES bending rigidity B value of less than or equal to
0.20 gf/cm.sup.2/cm; or (f) a co-efficient of friction of less than
0.45 MIU.
6. The sheet pack of claim 5 wherein the non-woven fabric comprises
a mixture of cotton, rayon, and synthetic fibers.
7. The sheet pack of claim 6 wherein the non-woven fabric comprises
25-75% pulp (cotton), 10-50% rayon, and 2-15% polyester.
8. The sheet pack of claim 5 wherein the impermeable layer is a
metallic foil having one or more of the following specifications:
(a) from about 98 to 100% aluminum, (b) a melting point of greater
than 650.degree. C. (c) a specific gravity of 2.5 to 3.0, (d) a
thickness ranging from 2 to 15 microns.
9. The sheet pack of claim 4 wherein the absorbent layer is bonded
to the impermeable layer by a bonding agent that is a synthetic
polymer having melting point ranging from 221 to 248.degree. C. and
a specific gravity of 915 to 935 kg/m.sup.3.
10. The sheet pack of claim 4 wherein the impermeable layer causes
the treatment composition to show at least a 10% improvement in
skin penetration of the treatment composition into the treatment
surface when compared to the skin penetration of the treatment
composition into the treatment surface with a sheet pack containing
the same absorbent layer but with no impermeable layer being bonded
to the absorbent layer.
11. The sheet pack of claim 4 wherein the absorbent layer is bonded
to the impermeable layer by a bonding agent which is low density
polyethylene.
12. The sheet pack of claim 1 wherein the ingredient that
stimulates the variably expressed gene is also a skin treatment
active.
13. The sheet pack of claim 1 wherein the treatment composition
contains an additional skin treatment active.
14. The sheet pack of claim 2 where the activator of CLOCK, PER,
CRY, or BMAL is one or more of: Cichoric acid, Echinacea extract,
Tripeptide-32, Tetrapeptide-26; or an Autophagy activator.
15. The sheet pack of claim 12 wherein the additional skin
treatment active is a DNA repair enzyme, a probiotic microorganism,
a proteasome activator, or combinations thereof.
16. The sheet pack of claim 1 for treating facial or body skin.
17. The sheet pack of claim 1 wherein the user instructions are to
apply the sheet pack to the skin at a time ranging from 1800 to
2400 hours.
18. The sheet pack of claim 15 wherein the user instructions are to
apply the sheet pack to the skin at a time ranging from 2000 to
2400 hours.
19. The sheet pack of claim 15 wherein the user instructions are to
apply the sheet pack to the skin at a time ranging from 1800 to
2400 hours for 1 to 60 minutes.
20. A method for making a sheet pack comprising the steps of: (a)
identifying a gene that is variably expressed over a 24 hour period
in native untreated skin cells, (b) forming a sheet pack comprised
of an absorbent layer and, optionally, an impermeable layer bonded
to the absorbent layer, (c) impregnating the absorbent layer with a
treatment composition containing at least one ingredient that
stimulates the gene in (a) above when topically applied to skin;
(d) packaging the sheet pack in a package containing user
instructions to apply the sheet pack to the skin a time when the
gene in (a) above is being maximally expressed in native untreated
skin cells
21. The method of claim 20 wherein the gene that is variably
expressed over a 24 hour period is maximally expressed at times
ranging from 1800 to 2400 hours and is one or more of PER, CLOCK,
BMAL, or CRY.
22. A method for treating skin with a sheet pack comprising the
steps of: (a) forming a sheet pack comprised of absorbent layer and
optionally bonded thereto an impermeable layer; (b) impregnating
the absorbent layer with a treatment composition containing at
least one ingredient that stimulates a gene that is variably
expressed over a 24 hour period in native skin cells when topically
applied thereto, (c) topically applying the sheet pack to the skin
at a time when same gene in (b) above is being maximally expressed
in native untreated skin cells.
Description
[0001] The invention is in the field of sheet packs impregnated
with treatment compositions for treatment of facial or body
surfaces to provide treatment benefits.
BACKGROUND OF THE INVENTION
[0002] The term "sheet pack" originally referred to a procedure
where a bed sheet soaked with water was wrapped around a person's
body. While the body gradually warmed the sheet the supposedly
agitated person was comforted by the warmth and cocoon of
surrounding fabric.
[0003] Today the term has a broader meaning, and in the beauty
industry refers to various sizes and shapes of fabric impregnated
with skin treatment compositions for temporary application to skin
to provide immediate benefits. Interestingly enough, the comfort
aspect of the original sheet packs remains, since today's products
are typically used during quiet and restful times of the day or at
night. In most cases, today's sheet packs are for facial treatment.
They are applied to the face and removed after a short period of
time which may range from 1 to 30 minutes. Thereafter the face can
either be cleansed or, if appropriate, any treatment composition
remaining on the skin is rubbed into the skin. These sheet packs
are particularly popular with Asian consumers and sometimes contain
active ingredients in larger concentrations than what is found in
the creams and lotions typically used as part of the day to day
beauty routine.
[0004] However, most sheet packs today are formulated with a
"kitchen sink" approach and contain many different active
ingredients that are touted to have a variety of benefits. There is
a failure to appreciate the difference between a treatment benefit
and the timing of that treatment benefit in order to maximize
efficacy. For example, it is known that in native skin cells,
expression of different genes is variable over a 24 hour cycle.
This is also referred to as circadian rhythms. Skin care products
will sometimes contain active ingredients that are said to
stimulate or inhibit expression of certain genes to ultimately
cause improvement in undesirable skin conditions such as aging,
hyper-pigmentation, moisturization, and so on. However, important
in maximizing the effectiveness of any treatment composition or the
active ingredients therein is timing. In particular, applying the
treatment composition to the treatment surface at a time when the
treatment surface is optimized to receive it ensures that the
treatment itself is maximally effective.
[0005] Accordingly, it is an object of the invention to provide a
sheet pack with optimized efficacy due to the presence of the sheet
pack constituents and a treatment composition that contains at
least one active that stimulates expression of a specific gene in
skin cells that is normally variably expressed in untreated native
skin cells and optionally at least one second skin treatment active
ingredient that provides a benefit; and where the sheet pack is
applied to the treatment surface (e.g. skin) at a time when the
ingredient in the treatment composition that stimulates expression
of the specific gene is being maximally expressed in the majority
of native untreated skin cells so that the treatment benefit of the
ingredient is optimized.
DEFINITIONS
[0006] All percentages stated herein are percentages by weight
unless otherwise indicated.
[0007] "BMAL" means the aryl hydrocarbon receptor nuclear
translocater-like protein 1 which is coded for by the ARNTL or BMAL
gene and affects circadian rhythms.
[0008] "CLOCK" means Circadian Locomotor Output Cycles Kaput gene,
present in skin cells, that codes for proteins (CLK) that impact
circadian rhythms, which are generally affected by light and
darkness.
[0009] "CRY" means cryptochrome circadian genes which codes for a
protein that affects circadian rhythms, both versions 1 and 2.
[0010] "PER" means the Period gene (1, 2, or 3) that encodes the
period circadian protein homolog protein in humans. Per1 in
particular is important to the maintenance of circadian rhythms and
ebbs and flows over a 24 hour cycle. Cellular Per1 gene expression
is most active at night, ebbs during daylight hours, and increases
again during periods of darkness.
[0011] "Sheet pack" means a thin sheet of material that may be
sized and shaped to fit a facial or body surface and is designed to
be applied for a temporary period of time to provide some cosmetic
or therapeutic improvement to the keratin surface such as skin in
the area where the pack was applied.
[0012] "Sheet mask" means a sheet pack which has been sized and
shaped for placement on the face, and may contain cut out portions
for the eyes, nose, or mouth.
[0013] "Benefit" means the benefit that a product, when used as
directed, is designed to provide. The product manufacturer's
advertised benefits (or claims) are generally what prompts the
consumer to buy the product to begin with. Benefits typically fall
into categories such as anti-aging treatment (treating lines and
wrinkles), anti-aging optics (blurring the appearance of skin
imperfections), moisturization (moisturizing dry skin),
anti-inflammation (treating irritated or inflamed skin to reduce
redness, pain, or heat), SPF (blocking UVA and/or UVB rays),
anti-acne (treating acne lesions, excessive skin oiliness), skin
whitening (whitening skin or improving hyperpigmented spots), and
so on.
DESCRIPTION OF THE DRAWINGS
[0014] FIG. 1 depicts an embodiment of the invention where the
sheet pack is in laminate form and the absorbent layer is bonded to
the impermeable layer with the bonding agent.
[0015] FIG. 2 depicts one type of apparatus that may be used to
create the laminate and bond the impermeable layer and absorbent
layer with the bonding agent.
[0016] FIG. 3 depicts a type of sheet pack in the form of a facial
treatment mask in two pieces--a piece designed for treatment of the
top half of the face and a second piece for application to the
bottom half of the face.
[0017] FIG. 4 depicts various types of packages and pouches in
which the sheet pack is contained and user instructions on the
optimum time to apply the sheet pack to the skin.
[0018] FIG. 5 depicts the results of testing untreated and ozone
exposed cells to determine PER1 activity over a 24 hour period.
[0019] FIG. 6 depicts the results of testing time synchronized
untreated cells, cells treated with Tripeptide-32 (a PER1 gene
activator), cells treated with ozone, and cells treated with ozone
and Tripeptide-32.
[0020] FIG. 7 depicts the results of penetration studies showing
that when the treatment composition is impregnated into the
laminate sheet mask of the invention the treatment composition
shows significantly improved (up to 25%) penetration into skin when
compared to the same sheet mask containing only an absorbent layer
and no impermeable layer.
SUMMARY OF THE INVENTION
[0021] The invention is directed to a sheet pack comprising an
absorbent layer impregnated with a treatment composition containing
at least one ingredient that when topically applied to skin
stimulates a gene that is variably expressed over a 24 hour period
in native untreated skin cells and optionally in combination with
at least one benefit agent; the sheet pack contained in a package
with user instructions to topically apply the sheet pack to the
skin at a select time period within the 24 hour time period when
the same gene that is stimulated by the ingredient is being
maximally expressed in native untreated skin cells.
[0022] The invention is also directed to a method for making a
sheet pack comprising the steps of:
[0023] (a) identifying a gene that is variably expressed over a 24
hour period in native untreated skin cells,
[0024] (b) forming a sheet pack comprised of an absorbent layer
and, optionally, an impermeable layer bonded to the absorbent
layer,
[0025] (c) impregnating the absorbent layer with a treatment
composition containing at least one ingredient that stimulates the
gene in (a) above when topically applied to skin;
[0026] (d) packaging the sheet pack in a package containing user
instructions to apply the sheet pack to the skin a time when the
gene in (a) above is being maximally expressed in the majority of
native untreated skin cells.
[0027] The invention is also directed to a method for treating skin
with a sheet pack comprising the steps of:
[0028] (a) forming a sheet pack comprised of absorbent layer and
optionally bonded thereto an impermeable layer;
[0029] (b) impregnating the absorbent layer with a treatment
composition containing at least one ingredient that stimulates a
gene that is variably expressed over a 24 hour period in native
skin cells when topically applied thereto,
[0030] (c) topically applying the sheet pack to the skin at a time
when same gene in (b) above is being maximally expressed in native
untreated skin cells.
DETAILED DESCRIPTION
[0031] The various components and embodiments of the invention will
be described in detail herein.
The Sheet Pack
[0032] The invention is directed to a sheet pack comprising an
absorbent layer and optionally an impermeable layer bonded to the
absorbent layer, where the absorbent layer is impregnated with a
treatment composition containing at least a one ingredient that has
activity in stimulating a gene that is variably expressed over a 24
hour period in native skin cells. This ingredient may also be a
skin treatment active, or it may be desirable to incorporate at
least one additional skin treatment active into the composition.
The sheet pack is contained in a package with user instructions to
topically apply the sheet pack to the skin at a time when the same
gene that is stimulated by the ingredient is being maximally
expressed in native untreated skin cells.
[0033] A. The Impermeable Layer
[0034] The sheet pack of the invention is in the form of a laminate
and optionally contains at least one impermeable layer. The term
"impermeable" means that the layer is generally impermeable to
moisture so that evaporation of the active formula from the sheet
mask absorbent layer may be substantially reduced or inhibited
entirely. The impermeable layer used in the laminate may be made of
metallic foil, synthetic polymeric materials, or natural polymeric
materials that are capable of existing in the form of a thin film.
Particularly preferred is metallic foil.
[0035] Metallic Foil
[0036] Suitable metallic foil may be a metal alloy containing
aluminum, silica, iron, copper, manganese, magnesium or zinc.
Preferred is aluminum foil from metal alloys containing 0.1 to 1.0%
of a combination of silica andiron, 0.01 to 0.12% copper, 0.001 to
0.06% Manganese, 0.001 to 0.06% Magnesium, 0.001 to 0.06% Zinc, and
greater than about 98% aluminum, preferably from about 98 to 100%
aluminum. The preferred aluminum foil is in a solid form, silver in
color, and has a melting point greater than 650.degree. C., and a
specific gravity ranging from 2.5 to 3.0, preferably about 2.7.
Most preferred is an aluminum foil having a thickness ranging from
2 to 15 microns, preferably from about 5 to 10 microns, more
particularly, about 7 microns. Most preferred is an aluminum foil
alloy made by Toyo KK, Osaka Japan.
[0037] Synthetic Polymer Sheets
[0038] Examples of impermeable layers suitable for preparation of
the laminate also includes polyvinylidene chloride, polyethylene,
or other homo- or copolymer of ethylenically unsaturated monomers
that are operable to form a film in thin sheets having a thickness
ranging from 2 to 20 microns. Examples of such impermeable layers
suitable for the laminate include polyvinylidene chloride or
polyethylene, of the kind often referred to by the trademark "Saran
Wrap" as set forth in Canadian Patent No. 385753. Preferred
synthetic polymeric impermeable layers have functional
characteristics similar to those of the metallic foil including a
specific gravity (density) ranging from 2.5 to 3.0, preferably
about 2.7.
[0039] The impermeable layer provides a barrier that aids in
penetration of active ingredients into the skin, reduces
evaporation of water and fluids from the mask, and generally
improves effectiveness of the treatment.
[0040] B. The Absorbent Layer
[0041] The absorbent layer used to create the sheet mask is
preferably made from nonwoven fabric. Non-woven fabrics refer to
those that are neither knitted nor woven. They are typically formed
by entangling fibers or filaments mechanically, thermally, or
chemically. Nonwoven fabrics suitable for the absorbent layer have
various preferred functional properties.
[0042] First, the most suitable nonwoven fabrics should have good
water or liquid absorption properties. That is, the fabric should
be capable of absorbing and retaining liquids. Suitable nonwoven
fabrics can be identified by measuring water absorption capability
according to the Larose method. In this case, examples of suitable
nonwovens may have water absorption readings ranging from about
0.03 to 2.5 ml/gram after 5 seconds per 1 gram. More preferred is
where the water absorption capacity ranges from 0.30 to 2.5
ml/gram. If the water absorption capacity is too low (below 0.03
ml/gram) the nonwoven fabric may not be capable of absorbing enough
of the treatment composition to treat the desired keratin surface
area. For example, in a face mask application, it is desired that
the absorbent layer contain from about 15 to 50 ml, more preferably
20-40 ml. Most preferred is a fill of about 24-25 ml. in a face
mask with a surface area ranging from 55 to 80 square inches.
[0043] In one preferred embodiment the nonwoven fabric has a
thickness ranging from 0.1 to 1.0 mm, preferably 0.2 to 0.8 mm,
more preferably from 0.5 to 0.7 mm.
[0044] Suitable nonwoven fabrics must also have a flexibility that
is sufficient to enable the fabric to readily drape onto the
treatment surface and remain in place on the treatment skin surface
even with slight movements. This property is typically quantified
by measuring bending resistance, preferably by the cantilever
stiffness method (IST 90.1-86 or ASTM D1388). In one embodiment the
nonwoven fabric may have a bending resistance of 1.0 to 2.0
mmm.sup.2/gram.
[0045] Another property of suitable nonwoven fabrics that can be
used in the invention is quantified by drape resistance. Suitable
nonwoven fabrics include those having a drape co-efficient ranging
from 1 to 70%, preferably from about 25-70% or 50-68%. The higher
the drape co-efficient, the less drapeable the fabric. In preparing
sheet packs for treating body surfaces, drape is an important
consideration. The sheet pack must be capable of draping on the
treatment surface.
[0046] In another embodiment, the KES bending rigidity B value of
the nonwoven fabric is 0.20 gf/cm.sup.2/cm or lower, and provides
fabric that is soft and easily bent.
[0047] In addition, one preferred embodiment of nonwoven may be
characterized by its friction co-efficient, which is one
measurement by which a smooth feel can be quantified. The formula
for calculating friction co-efficient is:
.mu.=F/N
wherein F is the force required to move an object on the horizontal
surface and N is the load normal to the surface. Friction is
preferably measured by the friction tester. In one preferred
embodiment the co-efficient of friction for the nonwoven fabric is
less than 0.45 MIU. Fabrics will measurements of greater than 0.45
MIU may tend to provide a hard feeling to the touch.
[0048] Examples of fibers that may be used to prepare the nonwoven
fabric of the absorbent material include cellulose, rayon, wool,
silk, cellulose acetate, synthetic or semi-synthetic fibers. Fibers
may also be composites of natural and synthetic fibers.
[0049] Cellulose fibers may be natural or synthetic. When the
cellulose fibers are hydrophilic the water absorption and retention
properties of the nonwoven fabric are improved. Examples of natural
cellulose fibers include wood pulp, pulp from non-wood sources,
cotton, cotton lint, etc. Pulp fibers may be from hard or soft wood
pulp and from bamboo, straw, tree bark, hemp, jute, and the like.
Soft wood pulp is particularly suitable because of its longer fiber
lengths which retain integrity during the bonding process used to
create nonwoven fabrics, where hard wood pulp, with its shorter
fiber length is not optimal. Particularly desirable are nonwoven
fabrics where the pulp comprises 5 to 90%, preferably 20-80%, more
preferably 40-70% of the nonwoven fabric composition.
[0050] It may be desirable to include rayon fibers in the nonwoven
fabric composition. Rayon, made from regenerated cellulose fibers,
will increase strength and water absorption in nonwoven fabrics.
The amount of rayon fibers may range from 10-90%, preferably from
20-80%, more preferably from 25-75% of the total nonwoven fabric
composition. Combining rayon and cellulose fibers provides a
nonwoven fabric with good feel, water absorption, and strength.
[0051] It may also be desirable to include synthetic fibers in the
nonwoven fabric. Examples of such synthetic fibers include homo-
and copolymers of polyamides, polyacrylonitriles, polyolefins,
polyesters, or polyvinyl alcohol such as polyethylene terephthalate
(PET), polytetramethylene teterphthalate (PTT), polypropylene, and
the like. If desired the nonwoven may contain from 1-75%,
preferably 5 to 50%, more preferably from about 5 to 30% of such
synthetic fibers. If the amount of synthetic fibers is too great,
e.g. greater than 60-70%, the water absorption of the nonwoven
fabric is decreased and the treatment composition is not readily
transferred to the treatment surface when the nonwoven fabric is
placed thereon. The transfer of the treatment composition
impregnated into the absorbent layer can be maximized if the
synthetic fibers are somewhat oleophilic. This causes the
moisturizing composition to be more readily exuded from the
absorbent layer into the skin. In one preferred embodiment the
synthetic fibers are PET.
[0052] Particularly preferred is where the absorbent layer is a
non-woven fabric containing about 25-75% pulp (cotton), 10-50%
rayon, and 2-15% polyester, more preferably about 55+/-5% pulp,
35+/-5% rayon, and 10%+/-5% polyester. An example of this non-woven
fabric can be purchased from Sansho Shigyo Co. Ltd. In other
preferred embodiments the fabric has one or more of the functional
parameters mentioned above, specifically, water absorption, drape
co-efficient, KES bending rigidity, and friction co-efficient.
[0053] C. The Bonding Agent
[0054] Lamination of the absorbent layer and the impermeable layer,
if desired, is accomplished with a bonding agent. The bonding agent
must secure the two layers together in permanent fashion, be
compatible with the impermeable and absorbent layers and the
treatment composition, and be operable to fuse the layers together
with application of pressure and heat. The heat used to effectuate
bonding must be low enough to effectively laminate the two layers
yet not high enough to cause burning, disintegration, melting, or
other disruption of the absorbent layer. In one embodiment the
bonding agent has a melting point ranging from 200 to 300.degree.
C. and may be operable to effectively fuse the absorbent layer and
the impermeable layer at a temperature that is from about 1 to 35%
less than its melting temperature. Most preferred is a polymer from
ethylenically unsaturated monomer repeat units such as acrylic
acid, methacrylic acid or their simple C1-20 alkyl or aromatic
esters; or ethylene, propylene, butylene repeat units. Particularly
preferred is polyethylene, in particular a low density polyethylene
sold by Tosoh Corporation under the trade name Petrothene which has
a melting point of 221 to 248.degree. C. and is in a solid form of
milky white pellets, with a specific gravity of 915 to 935
kg/m.sup.3. Most preferred is where the bonding agent has a melting
point ranging from 200 to 300.degree. C. and bonds the impermeable
layer to the absorbent layer at a temperature ranging from about
300 to 400.degree. C.
[0055] D. Bonding of the Absorbent and Impermeable Layers
[0056] In the case where the sheet pack is in laminate form, the
absorbent layer and the impermeable layer must be bonded together
to form a laminate where the absorbent layer is adhered to the
impermeable layer. The bonding is best achieved by placing an
extruder with the bonding material between two separate spools of
the nonwoven fabric and the metallic foil layer and extruding the
bonding material between the two layers with a sufficient amount of
pressure and heat to cause the layers to become laminated together,
then spooling the laminate onto a separate collecting roller.
[0057] The laminate 1 formed by bonding the absorbent layer 2 to
the impermeable layer 3 with the bonding agent 4 is depicted in
FIG. 1.
[0058] A suitable apparatus for performing the lamination is best
depicted in FIG. 2. The bonding material 17 is fed into the inlet
port 5 of the extruder 6. The nonwoven fabric 7 is on one spool 8
and the impermeable layer in the form of metallic foil 9 placed on
a second spool 10. When the apparatus is engaged, the nonwoven
fabric 7 is fed over guiding spools 11 and 12 that revolve and feed
the nonwoven film layer across over the two revolving spools 11 and
12 and onto a larger revolving spool 13 that abuts another larger
revolving spool 14 such that when spool 13 revolves in a clockwise
direction the spool 14 revolves in a counterclockwise direction and
the absorbent layer 7 and the metallic foil layer 9 are fed between
spools 13 and 14 and the bonding material 17 is fed between the two
layers with pressure and heat to cause the foil layer 9 and the
nonwoven fabric 7 to become bonded together.
[0059] Second spool 10, similarly revolves to feed metallic foil
layer 9 into spools 13 and 14. The metallic foil layer 9 is fed
from second spool 10 to larger spool 14 and pressure and heat
applied as the bonding material 17 is fed between the two layers to
bond them together and form the laminate 1. The laminate formed
when the bonded layers are fed out of spools 13 and 14 is fed along
smaller spool 15 and stored on receiving spool 18 for later cutting
into the desired sizes and shapes. The treatment composition (more
fully described below) can be impregnated into the absorbent layer
either before or after the laminate is cut into the desired shape
for the treatment surface.
[0060] More specifically, it is preferred that the temperature at
which the bonding of the layers mentioned above takes place ranges
from 300 to 400.degree. C., preferably from 325 to 360.degree. C.,
most preferably from 330 to 335.degree. C. The most optimal
pressure for the bonding ranges from 2.5 to 4.0 Pascal, more
preferably from 2.75 to 3.25 Pascal, most preferably from about 2.8
to 3.2 Pascal or in particular 3.0 Pascal.
[0061] The laminate formed from the nonwoven fabric layer, the
bonding agent layer, and the impermeable layer preferably has a
thickness ranging from 0.2 to 1.5 mm, preferably from about 0.2 to
1.0 mm, most preferably from 0.3 to 0.8 mm. This thickness provides
a sheet pack that has optimal strength and resiliency.
[0062] E. Impregnating Treatment Composition into the Absorbent
Layer
[0063] The treatment composition, more specifically described
herein, is preferably impregnated into the absorbent layer after
the lamination process either prior to cutting the laminated roll
into the desired shapes and sizes desired for the treatment surface
or after cutting the customized shapes. It is most preferred that
the impregnation of the treatment composition into the absorbent
layer occurs after the laminate has been cut into the desired size
and shape. In one embodiment of the invention the treatment
composition may be contained in a separate container and applied to
the mask by the consumer. In this case the sheet mask and a
container filled with the treatment composition are sold in the
form of a kit purchased by the consumer. Immediately prior to use
the consumer applies the treatment composition to the absorbent
layer of the mask for treatment of the skin.
[0064] F. The Sheet Mask Shapes
[0065] The laminate is then cut into the desired shapes depending
on the surface to be treated. For example, facial treatment sheet
packs can be cut in a variety of configurations suitable for
application to the face. These shapes include one piece masks that
cover the entire facial surface, or various smaller pieces that can
be placed in desired strategic areas such as under the eyes, around
the mouth, or on dry areas of skin.
[0066] Most preferred is a face mask in two sections as depicted in
FIG. 3, where a top portion covers the area between the forehead
and the nose and the bottom portion covers the around beneath the
nose and to the check or neck. The two piece mask of FIG. 3 has two
eye slits 19 that are large enough so that the upper section of the
mask 20 fits on the top part of the face but does not occlude the
eyes. Slits on either side of the nose 21 enable the mask portion
to treat the bridge area of the nose. The mask section for
treatment of the lower half of the face 22 has an open section 23
just large enough to surround the lips. Various slits 24, 25, 26,
and 27 are preferably embedded in lower face mask 22 to permit
easier draping around the chin.
[0067] The Sheet Pack Container and User Instructions
[0068] The sheet pack that is cut to fit the desired keratin
surface is the contained in a package which is preferably a
hermetic pouch or envelope 28 as depicted in FIG. 4. One type of
package is depicted in FIG. 4. The envelope for holding the sheet
pack may be of a size and shape to ensure that the sheet mask can
remain unfolded. Alternatively, it may be more desirable to fold
the sheet pack in halves or fourths and store in an envelope 28
that is smaller in size. The user instructions can be placed
directly on the envelope 29, or alternatively, on a secondary
package 30 in which one or more of the envelopes 28 are placed. The
secondary package may a box 30 for holding one or more individual
sheet packs contained in storage envelopes 28. The user
instructions instruct the user to apply the sheet pack at a time
when the same gene activated by the ingredient in the treatment
composition is being maximally expressed in native skin cells.
[0069] The Treatment Composition
[0070] The treatment composition used in the sheet pack of the
invention is preferably in liquid form. It may be an emulsion
(either oil in water or water in oil) or in a solution or
dispersion form. A particularly preferred form is referred to as a
serum, which is generally a mixture of water, humectants, and other
ingredients and contains very little to no oil phase. A suitable
treatment composition for impregnating into the sheet pack may have
a viscosity ranging from 2 to 1000, preferably from about 2 to 200,
more preferably from about 5-50 cps at 25.degree. C. and a specific
gravity ranging from 1.000 to 1.010, more preferably about 1.000 to
1.008, most preferably about 1.005. Maintaining the treatment
composition within the viscosity and specific gravity ranges
ensures that it will properly impregnate the absorbent layer and be
sufficiently liquid to permeate the layer but not so viscous to
create difficulty in permeating the layer.
[0071] If the treatment composition is in the form of an emulsion,
the composition may contain from about 1-99%, preferably from about
5-90%, more preferably from about 10-85% water and from about
1-99%, preferably from about 5-90%, more preferably from about
5-75% of oil. If in the form of an aqueous suspension or
dispersion, the composition may generally contain from about
1-99.9%, preferably from about 5-95%, more preferably from about
10-90% water, with the remaining ingredients being the active
ingredients or other formula ingredients.
[0072] Particularly suitable is a treatment composition that
contains at least one active ingredient that has activity in
stimulating a gene that is variably expressed over a 24 hour period
in native skin cells and optionally at least one skin treatment
active that provides a benefit. The composition may contain other
ingredients that contribute to providing a stable and commercially
acceptable formula.
[0073] The active ingredient that simulates the gene variably
expressed over a 24 hour period may act by synchronizing the
treated cells so that their biological (circadian) pathways are all
operating synchronously, particularly when the sheet pack is
applied consistently over time. Alternatively, this active
ingredient may also act by supplementing the depleted state of
native skin biological proteins that stimulate the variably
expressed gene; a condition often seen at the end of the day. The
ingredient with its activity in stimulating the variably expressed
gene will maximize the effectiveness of one or more benefit actives
so that their effects on the treatment surface are optimized.
[0074] A. The Active that Stimulates the Variably Expressed
Gene
[0075] Examples of variably expressed genes in skin cells include
period homolog genes (PER1, 2, and 3), Circadian Locomotor Output
Cycles Kaput (CLOCK), Chryptochrome Circadian Clock 1 or 1 (CRY1,
2), and Brain and Muscle Arylhydrocarbon Receptor Nuclear
Translocator (BMAL), etc. These genes are generally referred to as
circadian genes because they are variably expressed in skin cells
over a 24 hour period, with the peak expression usually occurring
in the evening to night time hours.
[0076] Active ingredients that stimulate expression of these genes
in skin cells (e.g. keratinocytes, fibroblasts, adipocytes, etc.)
may stimulate one or more of PER, CLOCK, CRY, or BMAL genes and
include, but are not limited to those set forth herein. The
ingredient that stimulates expression of the variably expressed
gene may be present in the treatment composition in amounts ranging
from 0.00001 to 8%, preferably from about 0.0005 to 5%, more
preferably from about 0.001 to 3%.
Echinacea--Cichoric Acid
[0077] Echinacea extract, or the active component derived
therefrom, cichoric acid has been shown to be a suitable activator
of PER and PER1 in particular. The cichoric acid component may be
synthetic or naturally derived. Synthetic cichoric acid may be
purchased from a number of commercial manufacturers including Sigma
Aldrich. Cichoric acid may also be extracted from botanical sources
that are known to contain cichoric acid such as Echinacea,
Cichorium, Taraxacum, Ocimum, Melissa, or from algae or sea
grasses. More specifically, botanical extracts such as Echinacea
purpurea, Cichorium intybus, Taraxacum officinale, Ocimum
basilicum, or Melissa officinalis are excellent sources. The term
"cichoric acid" when used herein also includes any isomers thereof
that are operable to increase PER1 gene expression in skin
cells.
[0078] Most preferred is a botanical extract from Echinacea
purpurea sold by Symrise under the brand name Symfinity.TM. 1298
which is an extract of Echinacea purpurea which is standardized
during the extraction process to contain about 3% by weight of the
total extract composition of cichoric acid. Echinacea extracts from
different sources will vary in cichoric acid content, and as such
will yield variable results in induction of per1 gene expression.
For example, we have observed that another component commonly found
in extracts of Echinacea, specifically caftaric acid, does not
increase PER1 gene expression in skin cells. Moreover, each species
of Echinacea will differ in content of phenolic and cichoric acids.
Ethanolic extract of the roots of Echinacea purpura will provide
more cichoric acid than ethanolic extracts of Echineacea
angustifolia or Echinacea pallida. The content of active
ingredients in any extract is also very dependent on the method of
extraction. For example, it is known that in many cases enzymatic
browning during the extraction process will reduce the phenolic
acid content of the resulting extract. The Echinacea extracts with
optimal cichoric acid content are preferably extracted in ethanol.
Alternate extractions may be water only, water and alcohols in
admixture, or alcohols alone with the alcohols selected from
methanol, ethanol, and those of similar lower carbon chain lengths
such as propanol, isopropanol, and so forth.
Peptides
[0079] A variety of peptides are suitable CLOCK or PER1 gene
activators. One example of such a peptide is disclosed in U.S.
Patent Application No. 2014/0045766 which is hereby incorporated by
reference in its entirety.
[0080] Such peptides have the general formula:
R.sub.1-(AA).sub.n-X.sub.1--S-T-P--X.sub.2-(AA).sub.p-R.sub.2
[0081] Where (AA).sub.n-X.sub.1--S-T-P--X.sub.2-(AA).sub.p is (SEQ
ID No. 1) and: [0082] X.sub.1 represents a threonine, a serine, or
is equal to zero, [0083] X.sub.2 represents an isoleucine, leucine,
proline, valine, alanine, glycine, or is equal to zero, [0084] AA
represents any amino acid or derivative thereof, and n and p are
whole numbers between 0 and 4, [0085] R.sub.1 represents the
primary amine function of the N-terminal amino acid, either free or
substituted by a protective grouping that may be chosen from either
an acetyl group, a benzoyl group, a tosyl group, or a
benzyloxycarbonyl group, [0086] R.sub.2 represents the hydroxyl
group of the carboxyl function of the C-terminal amino acid,
substituted by a protective grouping that may be chosen from either
a C.sub.1 to C.sub.20 alkyl chain or an NH.sub.2, NHY, or NYY group
with Y representing a C.sub.1 to C.sub.4 alkyl chain, [0087]
wherein the sequence of general formula (I) comprises from about 3
to 13 amino acid residues, [0088] said sequence of general formula
(I) possibly containing substitutions of amino acids X.sub.1 and
X.sub.2 with other chemically equivalent amino acids; [0089]
wherein the amino acids are: [0090] Alanine (A) [0091] Arginine (R)
[0092] Asparagine (N) [0093] Aspartic Acid (D) [0094] Cysteine (C)
[0095] Glutamic Acid (E) [0096] Glutamine (Q) [0097] Glycine (G)
[0098] Histidine (H) [0099] Isoleucine (I) [0100] Leucine (L)
[0101] Lysine (K) [0102] Methionine (M) [0103] Phenylalanine (F)
[0104] Proline (P) [0105] Serine (S) [0106] Threonine (T) [0107]
Tryptophan (W) [0108] Tyrosine (Y) [0109] Valine (V)
[0110] More preferred are peptides of the above formula as
follows:
TABLE-US-00001 (SEQ ID No. 1) S-T-P-NH.sub.2 Ser-Thr-Pro-NH.sub.2
(SEQ ID No. 2) Y-V-S-T-P-Y-N-NH.sub.2
Tyr-Val-Ser-Thr-Pro-Tyr-Asn-NH.sub.2 (SEQ ID NO. 3)
NH.sub.2-V-S-T-P-E-NH.sub.2 NH.sub.2-Val-Ser-Thr-Pro-Glu-NH.sub.2
(SEQ ID No. 4) NH.sub.2-L-H-S-T-P-P-NH.sub.2
NH.sub.2-Leu-His-Ser-Thr-Pro-Pro-NH.sub.2 (SEQ ID No. 5)
CH.sub.3NH-R-H-S-T-P-E-NH.sub.2
CH.sub.3-NH-Arg-His-Ser-Thr-Pro-Glu-NH.sub.2 (SEQ ID No. 6)
CH.sub.3NH-H-S-T-P-E-CH.sub.3NH
CH.sub.3-NH-His-Ser-Thr-Pro-Glu-CH.sub.3-NH
[0111] More preferred is the S-T-P--NH.sub.2 peptide, SEQ ID No. 1,
or mixtures thereof.
[0112] Most preferred is a peptide manufactured by ISP-Vincience
under the trademark Chronolux.RTM. having the INCI name
Tripeptide-32.
[0113] Another suitable peptide is as disclosed in U.S. Patent
Application No. 2011/0269694, hereby incorporated by reference in
its entirety and has the formula:
R.sub.1--X.sub.1--X.sub.2-Ser-Pro-Leu-Gln-X.sub.3--X.sub.4--R.sub.2
wherein: [0114] X.sub.1 is cysteine, a methionine or is equal to
zero, [0115] X.sub.2 is serine, threonine, or is equal to zero,
[0116] X.sub.3 is alanine, glycine, isoleucine, leucine, proline,
valine or is equal to zero. X.sub.4 is asparagine, glutamine, or is
equal to zero. [0117] R.sub.1 is the primary amine function of the
N-terminal amino.acid, either free or substituted by a protective
group which can be selected from an acetyl group, a benzoyl group,
a tosyl group or a benzyloxycarbonyl group, [0118] R.sub.2 is the
hydroxyl group of the carboxyl function of the C-terminal
amino.acid, either free or substituted by a protective group which
can be selected from a C1-20 alkyl chain or a NH.sub.2, NHY or NYY
group where Y is a C1-4 alkyl chain, said sequence of general
formula (I) being formed of 4 to 8 amino acid residues, said
sequence of general formula (I) possibly comprising substitutions
of amino acids X.sub.2 to X.sub.4 with other chemically equivalent
amino acids.
[0119] More preferred is a peptide wherein the substituents are
selected to provide the following:
Ser-Pro-Leu-Gln-NH.sub.2
[0120] This peptide may be purchased from ISP-Vinscience under the
trademark Chronogen.RTM. having the INCI name Tetrapeptide-26.
[0121] Also suitable as activators of one or more of PER, CLOCK,
BMAL, or CRY, are ingredients that are activators of the cellular
autophagy process. In general, the cellular autophagy process
comprises four general steps. Step 1 is the initiation of vacuole
formation; Step 2 the formation of the initial vacuole or
autophagosome which sequesters the cytoplasmic material to be
degraded. Step 3 is the maturation of the autophagosome into a
degradative vacuole. Step 4 is the actual degradation of the
sequestered material.
[0122] Ingredients with autophagy activation activity can be
identified by their ability to either stimulate or inhibit various
cellular metabolic pathways. For example, ingredients that
stimulate the expression of MAP-LC3, ATG5-12, protein p53, AMPK, or
DRAM genes are suitable autophagy activators. Ingredients that
inhibit the expression of mTOR genes are also suitable autophagy
activators.
[0123] The gene MAP-LC3 codes for microtubule-associated protein 1
light chain 3, a protein that initiates formation of
autophagosomes. ATG5-12 also stimulates formation of
autophagosomes. mTOR, also known as mammalian target of rapamycin,
is also known as the mechanistic target of rapamycin or FK506
binding protein 12-rapamycin associated protein 1 (FRAP1). FRAP1 is
encoded by the FRAP gene. Any ingredient that inhibits the
expression of mTOR, involved in autophagosome creation, will have
autophagy activating properties. Also suitable as autophagy
activators are ingredients that stimulate expression of protein
p53, AMPK, and/or DRAM (damage remedy autophagy modulator protein)
in keratinocytes. Protein p53, also known as a tumor suppressor
protein, is encoded by the p53 gene. AMPK means AMP activated
protein kinase and DRAM, damage related autophagy modulator. Both
are known to stimulate autophagy activation in keratinocytes.
[0124] Thus any ingredient that has the above mentioned effects on
the genes may be suitable autophagy activators and activators of
PER, BMAL, CLOCK, or CRY. During the autophagocytic process
cellular debris such as oxidized proteins and peroxidized lipids
are degraded. Such cellular debris often affects normal metabolic
function. Screening of ingredients to determine efficacy by ability
to stimulate or inhibit cellular, preferably keratinocyte, genes
and/or proteins mentioned above may be done according to methods as
set forth in US Patent Publication No. 2011/0243983, incorporated
by reference in its entirety, or other methods known in the
art.
[0125] For example, one general process for identifying ingredients
that may be autophagy activators is by first inducing nutritive
stress in cultured cells such as keratinocytes. For example, the
cells are first cultured in complete culture medium with growth
factors, for about 24 hours. The culture medium is then removed and
replaced with a non-nutritive culture medium, for example one that
does not contain growth factors. The cells are cultured for about
30 minutes to about 25 hours in a state of nutritive stress. Then,
the non-nutritive culture medium is removed and replaced with
complete culture medium to promote cellular recovery. Thereafter,
the cells are evaluated for autophagocytic activity by measuring
the expression of one or more of MAP-LC3; ATGS-12; phosphorylated
mTOR; phosphorylated p53; DRAM; or phosphorylated AMPK in those
cells. Measurement of such expression can take place by
immunofluorescence measurements. In addition, the expression can be
ascertained by Western Blot analysis of phosphorylated proteins
associated with the expressed genes.
[0126] Examples of ingredients that are known to exert either the
stimulatory or inhibitory effects on the above mentioned genes
which, in turn, stimulate autophagy and activate one or more of
PER, CLOCK, CRY, or BMAL, are yeast extracts including but not
limited to those from the genuses such as Lithothamnium, Melilot,
Citrus, Candida, Lens, Urtica, Carambola, Momordica, Yarrowia,
Plumbago, etc. Further specific examples include Lithothamniumn
calcareum, Melilotus officinalis, Citrus limonum, Candida saitoana,
Lens culinaria, Urtica dioica, Averrhoa carambola, Momordica
charantia, Yarrowia lipolytica, Plumbago zeylanica and so on.
[0127] Another ingredient that stimulates one or more of the above
genes is a certain oligosaccharide obtained by controlled enzymatic
depolymerization of membranous polysaccharides from brown seaweed
such as Laminaria digitata. More specifically, the oligosaccharide
is formed from urocanoic acids, in particular mannuronic acid and
guluronic acids. Most preferred is an active having the INCI name
"Hydrolyzed align" and having the CAS No. 73049-73-7.
[0128] The ingredient that stimulates that variably expressed gene
may, in and of itself, also be a skin treatment active.
Alternatively, the ingredient that stimulates the variably
expressed gene may have only that efficacy, and if so, it is
desirable to add one or more additional skin treatment actives.
This will ensure that stimulating the variably expressed gene at a
time when the gene is being maximally expressed in the majority of
native untreated skin cells provides a treatment benefit. In
particular, treatment benefits can be maximized in situations where
the skin cells are acting synchronously. Prior to cellular
synchronization, cellular biological pathways may not be running in
exact synchronicity. However, even if this is the case, it can be
said that normal circadian rhythms will cause most cells to be
metabolically operating in the same general time frame.
[0129] Other Skin Actives
[0130] The treatment composition preferably contains one or more
additional skin treatment actives. The skin treatment active may be
anything that provides a benefit, such as skin whitening agents
(via tyrosinase inhibition or other pathways), moisturizers,
anti-acne agents, anti-inflammatory agents, anti-rosacea agents,
cellular DNA repair actives, protein repair actives, anti-wrinkle
agents, skin firming agents, blurring agents, oil absorbing
actives, humectants, collagen or elastin stimulating actives, or
specific ingredients that directly or indirectly contribute to
providing the benefit. Such actives may be present in amounts
ranging from about 0.00001 to 10%, preferably from 0.00005 to 5%,
more preferably from about 0.0001 to 2%. Suitable benefit actives
include, but are not limited to those set forth herein. Preferred
are benefit actives that exhibit optimized efficacy when combined
with the ingredient that stimulates the variably expressed
gene.
DNA Repair Enzymes
[0131] The composition may contain one or more DNA repair enzymes.
Suggested ranges are from about 0.00001 to about 35%, preferably
from about 0.00005 to about 30%, more preferably from about 0.0001
to about 25% of one or more DNA repair enzymes.
[0132] DNA repair enzymes as disclosed in U.S. Pat. Nos. 5,077,211;
5,190,762; 5,272,079; and 5,296,231, all of which are hereby
incorporated by reference in their entirety, are suitable for use
in the compositions and method of the invention. One example of
such a DNA repair enzyme may be purchased from AGI/Dermatics under
the trade name Roxisomes.RTM., and has the INCI name Arabidopsis
Thaliana extract. It may be present alone or in admixture with
lecithin and water. This DNA repair enzyme is known to be effective
in repairing 8-oxo-Guanine base damage.
[0133] Another type of DNA repair enzyme that may be used is one
that is known to be effective in repairing 06-methyl guanine base
damage. It is sold by AGI/Dermatics under the tradename
Adasomes.RTM., and has the INCI name Lactobacillus ferment, which
may be added to the composition of the invention by itself or in
admixture with lecithin and water.
[0134] Another type of DNA repair enzyme that may be used is one
that is known to be effective in repairing T-T dimers. The enzymes
are present in mixtures of biological or botanical materials.
Examples of such ingredients are sold by AGI/Dermatics under the
tradenames Ultrasomes.RTM. or Photosomes.RTM.. Ultrasomes.RTM.
comprises a mixture of Micrococcus lysate (an end product of the
controlled lysis of various species of micrococcus), lecithin, and
water. Photosomes.RTM. comprise a mixture of plankton extract
(which is the extract of marine biomass which includes one or more
of the following organisms: thalassoplankton, green micro-algae,
diatoms, greenish-blue and nitrogen-fixing seaweed), water, and
lecithin.
[0135] Other suitable DNA repair enzymes include Endonuclease V,
which may be produced by the denV gene of the bacteriophage T4.
Also suitable are T4 endonuclease; O.sup.6-methylguanine-DNA
methyltransferases; photolyases such as uracil- and
hypoxanthine-DNA glycosylases; apyrimidinic/apurinic endonucleases;
DNA exonucleases, damaged-bases glycosylases (e.g.,
3-methyladenine-DNA glycosylase); correndonucleases either alone or
in complexes (e.g., E. coli uvrA/uvrB/uvrC endonuclease complex);
APEX nuclease, which is a multi-functional DNA repair enzyme often
referred to as "APE"; dihydrofolate reductase; terminal
transferase; topoisomerase; O.sup.6 benzyl guanine; DNA
glycosylases.
[0136] Other types of suitable DNA repair enzymes may be
categorized by the type of repair facilitated and include BER (base
excision repair) or BER factor enzymes such as uracil-DNA
glycosylase (UNG); single strand selective monofunctional uracil
DNA glycosylase (SMUG1); 3,N(4)-ethenocytosine glycosylase (MBD4);
thymine DNA-glycosylase (TDG); A/G-specific adenine DNA glycosylase
(MUTYH); 8-oxoguanine DNA glycosylase (OGG1); endonuclease III-like
(NTHL1); 3-methyladenine DNA glycosidase (MPG); DNA glycosylase/AP
lyase (NEIL1 or 2); AP endonuclease (APEX 1 and 2), DNA ligase
(LIG3), ligase accessory factor (XRCC1); DNA
5'-kinase/3'-phosphatase (PNKP); ADP-ribosyltransferase (PARP1 or
2).
[0137] Another category of DNA repair enzymes includes those that
are believed to directly reverse damage such as O.sup.6-MeG alkyl
transferase (MGMT); 1-meA dioxygenase (ALKBH2 or ALKBH3).
[0138] Yet another category of enzymes operable to repair
DNA/protein crosslinks includes Tyr-DNA phosphodiesterase
(TDP1).
[0139] Also suitable are MMR (mismatch exision repair) DNA repair
enzymes such as MutS protein homolog (MSH2); mismatch repair
protein (MSH3); mutS homolog 4 (MSH4); MutS homolog 5 (MSH5); or
G/T mismatch-binding protein (MSH6); DNA mismatch repair protein
(PMS1, PMS2, MLH1, MLH3); Postmeiotic segregation increased 2-like
protein (PMS2L3); or postmeiotic segregation increased 2-like 4
pseudogene (PMS2L4).
[0140] Also suitable are DNA repair enzymes are those known as
nucleotide excision repair (NER) enzymes and include those such as
Xeroderma pigmentosum group C-complementing protein (XPC); RAD23
(S. cerevisiae) homolog (RAD23B); caltractin isoform (CETN2); RFA
Protein 1, 2, of 3 (RPA1, 2, or 3); 3' to 5' DNA helicase (ERCC3);
5' to 3' DNA helicase (ERCC2); basic transcription factor (GTF2H1,
GTF2H2, GTF2H3, GTF2H4, GTF2H5); CDK activating kinase (CDK7,
CCNH); cyclin G1-interacting protein (MNAT1); DNA excision repair
protein ERCC-5l; excision repair cross-complementing 1 (ERCC1); DNA
ligase 1 (LIG1); ATP-dependent helicase (ERCC6); and the like.
[0141] Also suitable may be DNA repair enzymes in the category that
facilitate homologous recombination and include, but are not
limited to DNA repair protein RAD51 homolog (RAD51, RAD51L1, RAD51B
etc.); DNA repair protein XRCC2; DNA repair protein XRCC3; DNA
repair protein RAD52; ATPase (RAD50); 3' exonuclease (MRE11A); and
so on.
[0142] DNA repair enzymes that are DNA polymerases are also
suitable and include DNA polymerase beta subunit (POLB); DNA
polymerase gamma (POLG); DNA polymerase subunit delta (POLD1); DNA
polymerase II subunit A (POLE); DNA polymerase delta auxiliary
protein (PCNA); DNA polymerase zeta (POLZ); MAD2 homolog ((REV7);
DNA polymerase eta (POLH): DNA polymerase kappa (POLK): and the
like.
[0143] Various types of DNA repair enzymes that are often referred
to as "editing and processing nucleases" include 3'-nuclease;
3'-exonuclease; 5'-exonuclease; endonuclease; and the like.
[0144] Other examples of DNA repair enzymes include DNA helicases
including such as ATP DNA helicase and so on.
[0145] The DNA repair enzymes may be present as components of
botanical extracts, bacterial lysates, biological materials, and
the like. For example, botanical extracts may contain DNA repair
enzymes.
[0146] The compositions of the invention may contain one or more
DNA repair enzymes.
[0147] Proteasome Activators
[0148] The treatment composition may contain one more proteasome
activators in amounts ranging from about 0.0001 to 65%, preferably
from about 0.0005 to 50%, more preferably from about 0.001 to 40%.
Suitable proteasome activators are any compounds, molecules, or
active ingredients that stimulate proteasome activity in the cells
of keratin surfaces. Proteasomes are protein complexes within cells
that degrade damaged proteins. Ingredients that are proteasome
activators will stimulate proteasome activity in cells where such
activity may be reduced due to age, cellular damage such as what is
caused by exposure to UV light.
[0149] Examples of suitable proteasome activators include, but are
not limited to, algin, alginates, hydrolyzed algin, molasses
extract, Trametes extracts, including extracts from Trametes
versicolor, Olea Europa (Olive) fruit extract either alone or in
combination with Acacia senegal extract, Pomiferin/Osajin, plankton
extract, arginine ferulate, a composition comprising plankton
extract/butylene glycol/arginine ferulate/water, yeast extract,
Plankton extract, and a peptide referred to as UB5
(penta-ubiquitin).
[0150] Probiotic Microorganisms
[0151] The treatment composition may contain one or more probiotic
microorganisms or lysates or filtrates thereof. The probiotic
microorganism extract may be obtained from the fermentation of any
probiotic bacteria or yeast including those from the order
Lactobacillales or Bifidobacteriales, or the genus of yeast,
Saccharomyces. More preferred bacteria are from Bifidobacteriales
and Lactobacillales. Suitable bacteria from Lactobacillales order
include the lactic acid producing bacteria from Abiotrophia,
Aerococcus, Camobacterium, Enterococcus, Lactobacillus,
Lactococcus, Leuconostoc, Oenococcus, Pediococcus,
Sporolactobacillus, Teragenococcus genus and so on. Particularly
desirable are bacteria from the Lactobacillus genus, of which there
are a considerable number of species. Most preferred are
Lactobacillus Plantarum or Lactobacillus casei or rhamnosus. P
[0152] Suitable probiotics from Bifidobacteriales includes those
from the Bifidobacterium genus. Particularly preferred are those
from Bifidobacterium longum although other species may be suitable.
Particularly preferred are inactivated bacterial lysates from
Bifidobacterium longum which may be in the form of a fermentation
product. Such ingredients have the INCI names Bifida lysate, Bifida
ferment lysate, Bifida ferment filtrate. The Bifidobacterium may
also be in the form of a mixture with other botanical extracts or
ingredients, or in the form of a fermentation product.
[0153] Suitable probiotic yeasts include those from the genus
Saccharomyces, including species such as Saccharomyces cerevisiae.
boulardii, bulderi, and so on.
[0154] In one embodiment of the invention the Bifidobacterium is as
set forth in U.S. Pat. No. 6,790,434 which is hereby incorporated
by reference in its entirety.
[0155] In another embodiment of the invention the probiotic
microorganism extract used in the color cosmetic composition is
obtained as set forth in U.S. Pat. No. 7,510,734 which is hereby
incorporated by reference in its entirety, and has the CTFA name
Lactobacillus ferment, which is defined as an extract obtained from
the fermentation of Lactobacillus. Commercial sources include those
sold under the trade names AC Probiotic 1 by Active Concepts LLC or
Lactobacillus crispatus KLB 46 sold by Natural F&P Co., Ltd of
Korea. Also suitable are various derivatives including one having
the CTFA name Lactobacillus Ferment Filtrate, which is a filtrate
of the extract from Lactobacillus Ferment, which may be purchased
from Active Concepts LLC as a mixture of salicylic acid and the
filtrate sold under the trade name ACB Salicylic Acid Bioferment.
Also suitable are derivatives having the CTFA names Lactobacillus
Ferment Lysate which is a lysate of the extract from fermentation
of Lactobacillus, or Lactobacillus Ferment Lysate Filtrate where
the lysate of the extract from fermentation of Lactobacillus is
filtered.
[0156] Also suitable are extracts from yeast such as Saccharomyces
which are fermented alone or in combination with various plant
materials, for example, apple, ginseng, garlic, and so on. Such
ingredients have the CTFA names Saccharomyces Ferment,
Saccharomyces Ferment Lysate, Saccharomyces Ferment Lysate
Filtrate, Saccharomyces/grape ferment, Saccharomyces/Lamanaria
Saccharina ferment, and so on; as well as extracts obtained from
fermentation of Saccharomyces in combination with metals such as
copper, calcium, magnesium, tourmaline, and so on.
[0157] Suitable ranges of the probiotic microorganism or ferment or
lysate thereof may be from about 0.0001 to 35%, preferably from
about 0.001 to 20%, more preferably from about 0.01 to 10%.
Other Ingredients
[0158] Other ingredients may be present in the treatment
composition in order to provide a stable, cosmetically acceptable
composition. Such ingredients include surfactants, thickening
agents, preservatives, humectants, botanical extracts, other
peptides or proteins, and the like.
[0159] More specifically, suitable surfactants particularly include
nonionic organic or silicone based surfactants, preferably those
having an HLB ranging from 5 to 13. More specifically, alkoxylated
alcohols where the alkoxy group ranges from 1 to 26 carbon atoms,
preferably fatty alkoxylated alcohols from lauric, stearic,
behenic, or cetearyl alcohols. Examples include Laureth, Oleth,
Gluceth, or methyl or ethyl derivatives thereof. More specific
examples include PEG-75, methyl gluceth-20, Bis-PEG-18 methyl ether
dimethyl silane, glycereth-26, PEG-8 glyceryl isostearate, oleth-3
phosphate, Laureth-3 and mixtures thereof. If present the
surfactants may range from 0.01 to 10%.
[0160] Suitable thickening agents include aqueous or non-aqueous
thickening agents such as carbomers, C10-30 alkyl acrylates
crosspolymer, sodium polyacrylate, Polyacrylate crosspolymer-6,
Polyacrylate crosspolymer-7 and so on. If present, such thickening
agents may range from 0.1 to 10%.
[0161] Suitable humectants include alkylene glycols such as
butylene, pentylene, propylene glycols, ethyl hexyl glycerin,
glycerin and mixtures thereof. If present such humectants agents
may range from 0.1 to 5%.
[0162] The composition may also contain one or more botanical
ingredients such as Porio cocos sclerotium extract, Silybum
marianum, Anthemis nobilis, Magnolia officianalis bark extract,
Garcinia mangostana extract, Cladosiphon okamaranus extract, Betula
alba extract, Artemia extract, and mixtures thereof. Such extracts
may be present in amounts ranging from 0.001 to 5%, preferably from
about 0.01 to 3%, more preferably from about 0.01 to 1%.
[0163] Suitable treatment compositions may contain:
[0164] 50-95% water
[0165] 0.001-5% botanical extracts
[0166] 0.01-5% of the variable gene stimulating active,
[0167] 0.01-5% of the skin treatment active,
[0168] 0.01-5% of botanical extracts,
[0169] 0.01-5% humectants; and
[0170] 0.01-5% of a thickening agent.
[0171] Another suitable treatment composition may contain:
[0172] 50-95% water,
[0173] 0.01-5% of the variable gene stimulating active which is
also a skin treatment active,
[0174] 0.01-5% of a DNA repair enzyme; and
[0175] 0.01-5% of inactivated bacterial lysates from
Bifidobacterium.
The Methods
[0176] In the method of the invention the sheet pack is applied to
the desired keratin surface for a period of time ranging from 1 to
60 minutes. However, one particular benefit of the sheet pack is
that it provides effective skin treatment in 10 minutes or less.
Most standard sheet pack products require 20-30 minutes. The amount
of fill 24-25 ml. is perfect for treating a standard face having
20-40 square inches. The treatment composition remaining on the
face after removal of the mask can be massaged into the skin as a
treatment lotion or cream, and may obviate the need for applying
additional moisturizers to the skin. Especially during periods of
nightly rest, the skin barrier naturally becomes more permeable,
thus permitting optimized treatment of skin. In one preferred
embodiment the user instructions instruct the consumer to apply the
sheet mask during the period of 1200 to 2400 hours, more preferably
from 1600-2400, most preferably from 1800 to 2400 hours.
[0177] The invention also comprises a method for making a sheet
pack comprising the steps of:
[0178] (a) identifying a gene that is variably expressed over a 24
hour period in native untreated skin cells,
[0179] (b) forming a sheet pack comprised of an absorbent layer
and, optionally, an impermeable layer bonded to the absorbent
layer,
[0180] (c) impregnating the absorbent layer with a treatment
composition containing at least one ingredient that stimulates the
gene in (a) above when topically applied to skin;
[0181] (d) packaging the sheet pack in a package containing user
instructions to apply the sheet pack to the skin a time when the
gene in (a) above is being maximally expressed in native untreated
skin cells.
[0182] In step (a) the gene that is variably expressed over a 24
hour period in native untreated skin cells can be identified by the
method set forth in Example 1, or similar methods.
[0183] Once the gene that is identified in (a) is determined,
ingredients can be screened to determine their effect on gene
expression in various types of cells such as skin cells. The
ingredient that shows activity in stimulating the same gene
identified in (a) above is selected. That ingredient is then formed
into a treatment composition and impregnated into an absorbent
layer as further described herein. A sheet pack is prepared by
cutting the fabric into the desired shapes and packaging it into a
package that contains user instructions to apply the sheet pack to
the skin at time when the gene identified in (a) is being maximally
expressed in native untreated skin cells.
[0184] The invention is also directed to a method for treating skin
with a sheet pack comprising the steps of:
[0185] (a) forming a sheet pack comprised of absorbent layer and
optionally bonded thereto an impermeable layer;
[0186] (b) impregnating the absorbent layer with a treatment
composition containing at least one ingredient that stimulates a
gene that is variably expressed over a 24 hour period in native
skin cells when topically applied thereto,
[0187] (c) topically applying the sheet pack to the skin at a time
when same gene in (b) above is being maximally expressed in native
untreated skin cells.
[0188] The method of the invention is as described herein. The
invention will be further described in connection with the
following examples which are set forth for the purposes of
illustration only.
Example 1
[0189] Per1 gene expression in normal human epidermal keratinocytes
(NHEK) donors was tested in control cells and cells exposed to
ozone using the reporter assay. NHEK were plated at a concentration
of 3.times.10.sup.4 in a black walled, 96 well microtiter plate for
3 hours in EpiLife media. The cells were then transfected in
supplement free media with a plasmid that contained luciferase as
the reporter gene ligated upstream to a per1 promoter element. In
addition, transfection was facilitated by addition of Plus and
Lipfectamine reagents (Invitrogen, Carlsbad, Calif.). Transfection
in supplement free media was carried out for an additional four
hours. This "starves" the cells which in turn causes them to be
synchronized in their circadian rhythms. After transfection, full
media neat and containing ozone was added and incubated for 16
hours. Then a luciferase reagent, Glo-Bright (Promega Corporation,
Madison, Wis.) was added and luminescence measures in an Lmax
luminometer (Molecular Devices, Sunnyvale, Calif.). The results are
set forth in FIG. 5 and show that untreated cells show variable
Per1 activity over a 24 hour period with the maximum activity
occurring at time 0 (night) and slowly decreasing to its lowest
level 12 hours later (day), and then increasing again at 24 hours.
Ozone treated cells show a decrease in per1 activity at 0, 6, and
12 hours, with the cellular stabilization against the tox effects
of ozone stabilizing by 24 hours. The results demonstrate the
normal circadian rhythm of untreated cells as a function of per1
gene expression in NHEK.
[0190] The test was performed again, and in addition, a peptide
with per1 gene activity was tested. The results are set forth in
FIG. 6. At 0 time synchronized untreated cells, cells treated with
Tripeptide-32, cells treated with ozone, and cells treated with
ozone and Tripeptide-32 clearly show that Tripeptide-32 is a per1
gene activator and increases per1 gene expression in untreated
cells; and that this effect ameliorates the adverse effects found
in cells treated with ozone. At 6 and 12 hours, the Tripeptide-32
treated cells with and without ozone show improved per1 gene
expression when compared to untreated cells and cells treated with
just ozone. At 24 hours the cells treated with ozone and
Tripeptide-32 showed the highest level of per1 gene expression with
the untreated cells, Tripeptide-32 treated cells, and ozone treated
cells all showing lesser, and about equivalent, expression of
PER1.
[0191] In both tests, NHEK were treated at the start of the test (0
hours) so that they were all synchronized with respect to their
circadian rhythm, and expressing per1 at the same time. Over the 24
hour period, the level of per1 gene expression decreased to its
lowest point at 12 hours, which corresponds to mid-day. The per1
activity then increased at 24 hours. However, since the cells
synchronized at time 0 have not all maintained their synchronicity
in tandem, but rather have begun to diverge in their circadian
pathway, the increase in per1 gene expression is less than it was
at 0 hours. The results show the natural circadian rhythm of cells
over a 24 hour period and that expression of per1 increases at a
time that is consistent in a 24 hour cycle; usually at night.
Example 2
[0192] A treatment composition was prepared as follows:
TABLE-US-00002 Ingredient % by weight Water QS100 Methyl gluceth-20
4.40 PEG-75 4.00 Bis-PEG-18 Methyl Ether Dimethyl Silane 2.00
Butylene glycol 1.40 Propanediol 1.10 Glycereth-26 1.00 PEG-8
Glyceryl Isostearate 0.80 Glycine 0.50 Squalane 0.50 Algae extract
0.49 Oleth-3 phosphate 0.45 Preservatives 0.25 Tocopherol acetate
0.40 Caffeine 0.20 Carbomer 0.14 Dextrin 0.10 Sodium hyaluronate
0.07 Porio cocos Sclerotium extract 0.1 Xanthan gum 0.05 Hydrolyzed
rice extract 0.03 Echinacea purpura (Coneflower) extract 0.03
Laureth-3 0.03 Silybum marianum (Lady thistle) extract 0.02
Anthemis nobilis (Chamomile) extract 0.01 Hydroxyethylcellulose
0.01 Magnolia officinalis bark extract 0.01 Garcinia mangostana
peel extract 0.01 Yeast extract 0.06 Acetyl dipeptide-1 cetyl ester
0.005 Cladosiphon okamuranus extract 0.005 Glycerin 0.005 Artemia
extract 0.001 Betula alba (birch) extract 0.001 Hydrolyzed algin
0.0003 Lactobacillus ferment 0.0003 Lecithin 0.0003 Ethylhexyl
glycerin 0.0002 Coffee seed extract 0.0001
[0193] The composition was prepared by combining the ingredients
and mixing well.
Example 3
[0194] Non-woven fabric comprised of 45-65% (55%) pulp, 25-45%
(35%) rayon, and 5-15% (10%) polyester (Non-woven Fabric KP9650,
Sansho Shigyo Co. Ltd, Tosa City, Kochi, Japan) was cut into a
pattern for a face mask with holes for eyes, nose and mouth as
depicted in FIG. 3. A second face mask was prepared by preparing a
laminate of aluminum foil (Toyo Aluminum KK, Osaka Japan) comprised
of aluminum and aluminum alloys (about 99.30% or more aluminum,
0.7% or less of each of Silicon and Iron, 0.1% of less of Copper,
0.05 or less of Manganese, 0.05% or less of Magnesium, and 0.05% or
less of Zinc) with the same non-woven fabric. The non-woven fabric
was loaded onto one spool. The aluminum foil onto a second spool.
An extruder containing low density polyethylene (Petrothene, Tosoh
Corporation, Tokyo Japan) extruded the resin between the two films
which were compressed between a pressure bonding roller and a
cooling roller as depicted in FIG. 2. A second sheet pack of the
same design as in FIG. 2 was cut from the laminated film. The
composition of Example 2 was impregnated into the non-woven layer
of both sheet masks.
[0195] The masks were then tested for their efficacy in penetrating
skin on skin models.
Fluorescein Skin Model Test
[0196] Migration of fluorescein through EFT-400 skin models into
the media was measured using a fluorescent plate reader at specific
time points (at t=0, 15 30 45, 60, 90, 120, 150, 180 min) and
results were compared. A more penetrating effect attributed to the
mask suggested more fluorescein migration into the media.
[0197] Materials: [0198] EFT-400 Living Skin Equivalents: Mattek;
EFT-400; Lot#17586; Kit E. ("LSE") [0199] EFT 400 Media: Mattek;
EFT-400-asy; Lot#092914GSA. [0200] Fluorescein: Vendor: Sigma Cat#
F6377-100G Lot#061M0048V [0201] DPBS (Dulbecco's Phosphate Buffered
Saline): Vendor: Corning Cellgro Cat#21-0341-CV Lot#21031456.
[0202] Masks Provided: [0203] Face mask with absorbent layer only
from non-woven fabric containing 55+/-5% pulp, 35+/-5% rayon, and
10%+/-5% polyester. Fabric purchased from Sansho Shigyo Co.
Ltd.
[0204] Face mask with same absorbent layer as noted above, and in
addition, an impermeable layer of metallic aluminum foil having a
thickness of about 7 microns, purchased from Toyo KK, Osaka Japan.
The two layers were bonded together as noted herein with low
density polyethylene. [0205] Dermal Biopsy Punch 8 mm (to cut
pieces out of masks in 8 mm round circles to fit inside well of
EFT-400)
[0206] Samples Tested: n=2 [0207] Blank--nothing applied to LSE
(living skin equivalent) [0208] 25 ul DPBS only applied topically
to LSE [0209] 25 ul Fluorescein @ 100 ppm diluted in DPBS applied
topically to LSE [0210] Absorbent layer only mask was layered over
the LSE onto which 25 ul of Fluorescein @100 ppm was placed [0211]
Mask of laminate of absorbent layer and impermeable layer was
layered over the LSE onto which 25 ul of Fluorescein @100 ppm was
placed
[0212] Procedure
[0213] Assembled and fed 2.5 ml Media (EFT-400), and incubated
overnight at standard conditions (5% CO.sub.2/37.degree. C./100%
humidity). Maintained LSE's as per MatTek's EpiDerm Full Thickness
400 (EFT-400) Use Protocol. [0214] 1. Aspirated out existing Media
and refreshed LSE's with 2.5 ml Media per well. [0215] 2. Using 8
mm biopsy punch small circles are cut neatly out of the provided
samples as noted above [0216] 3. Pipetted 25 ul of DPBS on top of
LSE on top of designated wells [0217] 4. Pipetted 25 ul of
Fluorescein in DPBS only (100 ppm) on top of LSE [0218] 5. Placed
the die-cut absorbent layer only circle into the LSE well and
pipetted 25 ul of 100 ppm Fluorescein in DPBS onto the fabric of
the mask; also with wells containing DPBS only control [0219] 6.
Picked up die-cut laminate of absorbent layer and impermeable
layer. While holding the circle over the well, saturated the
absorbent layer with 25 ul of 100 ppm Fluorescein in DPBS. Then
quickly apply die-cut mask piece soaked disk with soaked side down
into EFT well. [0220] 7. Supernatant was drawn out of the bottom
well of the LSE at various time-points as indicated below and read
using fluorescent analysis via plate-reader following final read
(t=3 hr). [0221] i. Settings used were: Bottom Read Ex: 494 em: 521
Cutoff 515
[0222] Collected 250 ul of supernatant at the following time-points
and stored in 0.5 ul micro-centrifuge tubes (store protected from
light, at 4.degree. C.) for fluorescent plate-read following 3 hour
time-point in minutes: 0, 15, 30, 45, 60, 90, 120, 150, and
180.
[0223] A standard curve was created using a serial dilution of 100
ppm Fluorescein diluted in EFT-400-ASY Media and pipetting 100 ul
of each dilution into the wells of a 96-well plate as per the
template below. Two plates were prepared: one for the standard
curve measurements and one for the test samples. Preparing Standard
Curve Samples (n=2):
[0224] Utilizing eight 1.5 ul Eppendorf tubes a serial dilution set
was created: [0225] Pipette 1,000 ul of 100 ppm Fluorescein in
Media EFT-400media in tube #1 [0226] In tubes 2-8 add in 500 ul of
EFT-400-ASY Media only [0227] Starting with tube #1 transfer 500 ul
of 100 ppm Fluorescein from tube 1 into tube 2 and pipette up and
down to mix thoroughly to create a final concentration in Tube#2 of
50 ppm. [0228] Then, after thoroughly mixed, pipette 500 ul from
tube #2 and deliver into tube #3, pipette up and down to mix
thoroughly. Creating a final concentration in Tube#3 of 25 ppm
[0229] Continue this serial transfer for remaining tubes, each
series dilution reducing the concentration in the following tubes
by half [0230] Pipette 100 ul of solution per well from each tube
to the corresponding wells of the 96 well plate
[0231] A second plate with each sample at each time-point is
created and read right after the standard curve 100 ul n=1.
Hour-Sample
[0232] A=nothing in well B=nothing in well C=25 ul DPBS only D=25
ul DPBS only well E=25 ul 100 ppm Fluorescein in DPBS well F=25 ul
100 ppm Fluorescein in DPBS well G=25 ul 100 ppm Fluorescein on
absorbent layer only well H=25 ul 100 ppm Fluorescein on absorbent
layer only well I=25 ul 100 ppm Fluorescein on full mask well J=25
ul 100 ppm Fluorescein on full mask well
[0233] The results were calculated and are graphically demonstrated
in FIG. 7. The sheet mask comprised of a laminate of a metallic
foil layer bonded to an absorbent layer showed consistently
improved skin penetration when compared to the mask comprised only
of the non-woven layer absorbent layer. Skin penetration means that
the ingredients present in the composition were actually absorbed
into the skin. While an impermeable layer may or may not cause less
evaporation of the treatment composition from the skin during the
period of use, this does not necessarily correlate with
penetration. For example, the treatment composition could simply
remain superficially on the skin surface.
[0234] While the invention has been described in connection with
the preferred embodiment, it is not intended to limit the scope of
the invention to the particular form set forth but, on the
contrary, it is intended to cover such alternatives, modifications,
and equivalents as may be included within the spirit and scope of
the invention as defined by the appended claims.
Sequence CWU 1
1
8113PRTArtificial SequenceCLOCK and/or PER1 gene activator 1Xaa Xaa
Xaa Xaa Xaa Ser Thr Pro Xaa Xaa Xaa Xaa Xaa 1 5 10 27PRTArtificial
SequenceCLOCK and/or PER1 gene activator 2Tyr Val Ser Thr Pro Tyr
Asn 1 5 35PRTArtificial SequenceCLOCK and/or PER1 gene activator
3Val Ser Thr Pro Glu 1 5 46PRTArtificial SequenceCLOCK and/or PER1
gene activator 4Leu His Ser Thr Pro Pro 1 5 56PRTArtificial
SequenceCLOCK and/or PER1 gene activator 5Arg His Ser Thr Pro Glu 1
5 65PRTArtificial SequenceCLOCK and/or PER1 gene activator 6His Ser
Thr Pro Glu 1 5 78PRTArtificial SequenceSynthetic peptide 7Xaa Xaa
Ser Pro Leu Gln Xaa Xaa 1 584PRTArtificial SequenceSynthetic
peptide 8Ser Pro Leu Gln 1
* * * * *